Phosphopeptide analysis by positive and negative ion matrix‐assisted laser desorption/ionization mass spectrometry

Abstract
This article describes a simple procedure for the detection of phosphorylated peptides by comparable positive and negative ion mode matrix-assisted laser desorption/ionization mass spectrometry measurements. Based on studies with phosphorylated peptides (EAIXAAPFAK, X = pS, pT, pY) and their corresponding non-phosphorylated analogs, it was found that phosphopeptides, which are characterized by a low ionization efficiency in the positive ion mode, exhibit drastically increased signal intensities in the negative ion mode compared to their non-phosphorylated analogs. The effect was successfully used to identify phosphorylated sequences of the commonly used phosphoprotein standards, protein kinase A and β-casein, by peptide mass fingerprint analyses of the corresponding Lys C and trypsin digests using both (positive and negative) ion modes. The comparison of positive and negative ion spectra of a given protein digest (relative intensity[M − H]−/relative intensity[M + H]+) can be used to identify any phosphopeptides present which may then be separated and analyzed further. Copyright © 2001 John Wiley & Sons, Ltd.

This publication has 17 references indexed in Scilit: